2018
Abl2 is recruited to ventral actin waves through cytoskeletal interactions to promote lamellipodium extension
Zhang K, Lyu W, Yu J, Koleske AJ. Abl2 is recruited to ventral actin waves through cytoskeletal interactions to promote lamellipodium extension. Molecular Biology Of The Cell 2018, 29: 2863-2873. PMID: 30256707, PMCID: PMC6249870, DOI: 10.1091/mbc.e18-01-0044.Peer-Reviewed Original ResearchConceptsCytoskeletal interactionsLamellipodium extensionTotal internal reflection fluorescence microscopyActin-rich structuresActin wavesActin-rich protrusionsN-terminal halfC-terminal halfNonreceptor tyrosine kinaseReflection fluorescence microscopyFoci colocalizeComplementation analysisLamellipodia protrusionKnockout cellsLamellipodium tipActin filament stabilizerCell shapeBind actinTyrosine kinaseCortactinABL2Fluorescence microscopyIntegrin β3High spatiotemporal resolutionPaxillin
2012
Structural Basis for Paxillin Binding and Focal Adhesion Targeting of β-Parvin*
Stiegler AL, Draheim KM, Li X, Chayen NE, Calderwood DA, Boggon TJ. Structural Basis for Paxillin Binding and Focal Adhesion Targeting of β-Parvin*. Journal Of Biological Chemistry 2012, 287: 32566-32577. PMID: 22869380, PMCID: PMC3463362, DOI: 10.1074/jbc.m112.367342.Peer-Reviewed Original ResearchConceptsΒ-parvinFocal adhesionsPaxillin bindingΑ-parvinFocal adhesion targetingN-terminal α-helixPaxillin LD1 motifCalponin homology domainFirst molecular detailsHigh sequence similarityCytoplasmic adaptor proteinIntegrin-linked kinasePaxillin LD1Co-crystal structureLD4 motifSignificant conformational flexibilityHomology domainAdaptor proteinCellular functionsSequence similarityRepeat motifsProper localizationMolecular detailsPaxillinStructural basis
2010
Crystal Structure of CCM3, a Cerebral Cavernous Malformation Protein Critical for Vascular Integrity*
Li X, Zhang R, Zhang H, He Y, Ji W, Min W, Boggon TJ. Crystal Structure of CCM3, a Cerebral Cavernous Malformation Protein Critical for Vascular Integrity*. Journal Of Biological Chemistry 2010, 285: 24099-24107. PMID: 20489202, PMCID: PMC2911348, DOI: 10.1074/jbc.m110.128470.Peer-Reviewed Original ResearchMeSH KeywordsApoptosis Regulatory ProteinsBinding, CompetitiveBrainCrystallography, X-RayDimerizationHemangioma, Cavernous, Central Nervous SystemHumansKineticsMembrane ProteinsMolecular ConformationMutationPaxillinProtein ConformationProtein FoldingProtein Structure, SecondaryProtein Structure, TertiaryProto-Oncogene ProteinsConceptsN-terminal dimerization domainPaxillin LD motifsCerebral cavernous malformationsAlpha-helical proteinsLD motifsCCM complexHomology domainFocal adhesionsDimerization domainMolecular basisHydrophobic pocketHuman populationCCM3 mutationsMutationsCCM3Crystal structureVascular integrityCCM2DomainPaxillinProteinMotifCCM1InteractionCells
2007
RhoA required for acid-induced stress fiber formation and trafficking and activation of NHE3
Yang X, Huang HC, Yin H, Alpern RJ, Preisig PA. RhoA required for acid-induced stress fiber formation and trafficking and activation of NHE3. American Journal Of Physiology. Renal Physiology 2007, 293: f1054-f1064. PMID: 17686951, DOI: 10.1152/ajprenal.00295.2007.Peer-Reviewed Original ResearchMeSH KeywordsAmidesAnimalsBenzoquinonesCell LineEnzyme InhibitorsExocytosisFocal Adhesion Kinase 1Hydrochloric AcidHydrogen-Ion ConcentrationLactams, MacrocyclicOpossumsPaxillinPhosphorylationProtein-Tyrosine KinasesPyridinesrhoA GTP-Binding ProteinRifabutinSodium-Hydrogen Exchanger 3Sodium-Hydrogen ExchangersStress FibersTyrosineConceptsStress fiber formationTyrosine phosphorylationFiber formationFocal adhesion proteinsApical membraneRho-kinaseNHE3 activityExocytic traffickingActivation of NHE3Exocytic processFocal adhesionsNHE3 exocytosisAdhesion proteinsStress fibersProtein abundancePaxillinPhosphorylationMicrofilament structureAntiporter activityKinaseRho-kinase inhibitorKinase inhibitorsTraffickingAbundanceNHE3 activation
2002
A Fragment of Paxillin Binds the α4Integrin Cytoplasmic Domain (Tail) and Selectively Inhibits α4-Mediated Cell Migration*
Liu S, Kiosses WB, Rose DM, Slepak M, Salgia R, Griffin JD, Turner CE, Schwartz MA, Ginsberg MH. A Fragment of Paxillin Binds the α4Integrin Cytoplasmic Domain (Tail) and Selectively Inhibits α4-Mediated Cell Migration*. Journal Of Biological Chemistry 2002, 277: 20887-20894. PMID: 11919182, DOI: 10.1074/jbc.m110928200.Peer-Reviewed Original ResearchConceptsCytoplasmic domainPaxillin interactionCell migrationIntegrin-mediated cell adhesionIntegrin alpha subunitsEnhanced cell migrationPaxillin bindingFunctional responseFocal adhesionsCellular functionsPaxillinCardiac developmentAlanine substitutionsMutational analysisAdaptor moleculeAcid regionAlpha subunitBiological processesCell spreadingCellular responsesCell adhesionIntegrin subunitsSubunitsTernary complexFragments
1998
Integrins Regulate the Association and Phosphorylation of Paxillin by c-Abl*
Lewis J, Schwartz M. Integrins Regulate the Association and Phosphorylation of Paxillin by c-Abl*. Journal Of Biological Chemistry 1998, 273: 14225-14230. PMID: 9603926, DOI: 10.1074/jbc.273.23.14225.Peer-Reviewed Original ResearchConceptsC-AblCell adhesionTyrosine kinaseFocal adhesion protein paxillinNon-receptor tyrosine kinasePhosphorylation of paxillinC-Abl kinaseEffects of integrinsFocal adhesionsProtein paxillinIntegrin regulationPaxillinTransient recruitmentKinaseIntegrinsCell functionProteinAdhesionPhosphorylationTyrosineRegulationABLRecruitmentActivationLocalization
1996
Role of tyrosine kinase pathways in ETB receptor activation of NHE3
Chu TS, Tsuganezawa H, Peng Y, Cano A, Yanagisawa M, Alpern RJ. Role of tyrosine kinase pathways in ETB receptor activation of NHE3. American Journal Of Physiology 1996, 271: c763-c771. PMID: 8843705, DOI: 10.1152/ajpcell.1996.271.3.c763.Peer-Reviewed Original ResearchConceptsET-1-induced tyrosine phosphorylationTyrosine kinase pathwayTyrosine phosphorylationKinase pathwayFocal adhesion proteinsIntegral membrane proteinsAntiporter activityClonal cell linesFocal adhesionsMembrane proteinsReceptor activationAdhesion proteinsImmunoprecipitation studiesPhosphorylationCytochalasin DET-1-induced increaseApical membraneDependent pathwayAntiporter activationProteinPaxillinP125FAKCell linesPhosphoproteinPathwayTyrosine phosphorylation of pp125FAK and paxillin in aortic endothelial cells induced by mechanical strain
Yano Y, Geibel J, Sumpio BE. Tyrosine phosphorylation of pp125FAK and paxillin in aortic endothelial cells induced by mechanical strain. American Journal Of Physiology 1996, 271: c635-c649. PMID: 8770005, DOI: 10.1152/ajpcell.1996.271.2.c635.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAortaCattleCell Adhesion MoleculesCell MovementCells, CulturedCytoskeletal ProteinsEndothelium, VascularFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine KinasesGenisteinIsoflavonesNitrilesPaxillinPhosphoproteinsPhosphorylationPhosphotyrosineProtein-Tyrosine KinasesStress, MechanicalTissue DistributionTyrosineTyrphostins
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